메뉴 건너뛰기




Volumn 106, Issue 1, 2012, Pages 1-17

Evaluation of solute binding to proteins and intra-protein distances from steady state fluorescence measurements

Author keywords

Albumin; Binding; Fluorescence; Resonance energy transfer

Indexed keywords

BOVINE SERUM ALBUMIN; FLUORESCENT DYE; FLUOROPHORE; HUMAN SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 84155167320     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2011.11.002     Document Type: Review
Times cited : (30)

References (143)
  • 1
    • 0022291011 scopus 로고
    • Measurement of ligand binding to proteins by fluorescence spectroscopy
    • L.D. Ward Measurement of ligand binding to proteins by fluorescence spectroscopy Methods Enzymol. 117 1985 400 414
    • (1985) Methods Enzymol. , vol.117 , pp. 400-414
    • Ward, L.D.1
  • 2
    • 79959690715 scopus 로고    scopus 로고
    • Fluorescence quenching and ligand binding: A critical discussion of a popular methodology
    • M. van de Weert, and L. Stella Fluorescence quenching and ligand binding: a critical discussion of a popular methodology Mol. Struct. 998 2011 144 150
    • (2011) Mol. Struct. , vol.998 , pp. 144-150
    • Van De Weert, M.1    Stella, L.2
  • 3
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • A.A. Bhattacharya, T. Grûne, and S. Curry Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin J. Mol. Biol. 303 2000 721
    • (2000) J. Mol. Biol. , vol.303 , pp. 721
    • Bhattacharya, A.A.1    Grûne, T.2    Curry, S.3
  • 5
    • 0016801988 scopus 로고    scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • G. Sudlow, D.J. Birkett, D.N. Wade, The characterization of two specific drug binding sites on human serum albumin, Mol. Pharmacol. 11 (l175) 824-832.
    • Mol. Pharmacol. , vol.11 , Issue.L175 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 6
    • 37049080392 scopus 로고
    • Experimental correction for the inner-filter effect in fluorescence spectra
    • M. Kubista, R. Sjöback, S. Ericsson, and B. Albinsson Experimental correction for the inner-filter effect in fluorescence spectra Analyst 119 1994 417 419
    • (1994) Analyst , vol.119 , pp. 417-419
    • Kubista, M.1    Sjöback, R.2    Ericsson, S.3    Albinsson, B.4
  • 7
    • 77749337740 scopus 로고    scopus 로고
    • Interaction studies of coumaroyltyramide with human serum albumin and its biological importance
    • S. Neelan, M. Gokara, B. Sudhamalla, D.G. Amooru, and R. Subramanyam Interaction studies of coumaroyltyramide with human serum albumin and its biological importance J. Phys. Chem. B 114 2010 3005 3012
    • (2010) J. Phys. Chem. B , vol.114 , pp. 3005-3012
    • Neelan, S.1    Gokara, M.2    Sudhamalla, B.3    Amooru, D.G.4    Subramanyam, R.5
  • 8
    • 70350107698 scopus 로고    scopus 로고
    • Investigation of the interaction of newly designed anticancer Pd (II) complexes with different aliphatic tails and human serum albumin
    • A. Divsalr, M.J. Bagheri, A.A. Saboury, H. Mansoori-Torshizi, and M. Amani Investigation of the interaction of newly designed anticancer Pd (II) complexes with different aliphatic tails and human serum albumin J. Phys. Chem. B 113 2009 14035 14042
    • (2009) J. Phys. Chem. B , vol.113 , pp. 14035-14042
    • Divsalr, A.1    Bagheri, M.J.2    Saboury, A.A.3    Mansoori-Torshizi, H.4    Amani, M.5
  • 9
    • 27744522469 scopus 로고    scopus 로고
    • Spectroscopic studies of the interaction of anti-coagulant rodenticide diphacinone with human serum albumin
    • DOI 10.1016/j.molstruc.2005.07.023, PII S0022286005005703
    • J. Tang, S. Qi, and X. Chen Spectroscopic studies on the interaction of anti-coagulant redenticide diphacinone with human serum albumin J. Mol. Struct. 79 2005 87 95 (Pubitemid 41586590)
    • (2005) Journal of Molecular Structure , vol.779 , Issue.1-3 , pp. 87-95
    • Tang, J.1    Qi, S.2    Chen, X.3
  • 10
    • 77950825780 scopus 로고    scopus 로고
    • Investigation on the interaction of prulifloxacin with human serum albumin: A spectroscopic analysis
    • Y.-B. Huang, S.-J. Wang, Y.-Q. Zi, S. Yu, X.-Y. Gao, and Y.-C. Tang Investigation on the interaction of prulifloxacin with human serum albumin: a spectroscopic analysis Chem. Pharm. Bull. 58 2010 582 586
    • (2010) Chem. Pharm. Bull. , vol.58 , pp. 582-586
    • Huang, Y.-B.1    Wang, S.-J.2    Zi, Y.-Q.3    Yu, S.4    Gao, X.-Y.5    Tang, Y.-C.6
  • 11
    • 38749086886 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin
    • DOI 10.1016/j.ijpharm.2007.09.016, PII S0378517307007703
    • N. Wang, L. Ye, F. Yan, and R. Xu Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin Int. J. Pharm. 351 2008 55 60 (Pubitemid 351186841)
    • (2008) International Journal of Pharmaceutics , vol.351 , Issue.1-2 , pp. 55-60
    • Wang, N.1    Ye, L.2    Yan, F.3    Xu, R.4
  • 12
    • 77952495197 scopus 로고    scopus 로고
    • Interactions of human serum albumin with phenotiazine drugs: Insights from fluorescence spectroscopic studies
    • H.-X. Bai, X.-H. Liu, F. Yang, and X.-R. Yang Interactions of human serum albumin with phenotiazine drugs: insights from fluorescence spectroscopic studies J. Chin. Chem. Soc. 56 2009 69 702
    • (2009) J. Chin. Chem. Soc. , vol.56 , pp. 69-702
    • Bai, H.-X.1    Liu, X.-H.2    Yang, F.3    Yang, X.-R.4
  • 14
    • 77949534896 scopus 로고    scopus 로고
    • Study on the interaction of 2-carboxyphenoxathiine with bovine serum albumin and human serum albumin by fluorescence spectroscopy and circular dichroism
    • A. Varlan, and M. Hillebrand Study on the interaction of 2-carboxyphenoxathiine with bovine serum albumin and human serum albumin by fluorescence spectroscopy and circular dichroism Rev. Roum. Chim. 55 2010 69 77
    • (2010) Rev. Roum. Chim. , vol.55 , pp. 69-77
    • Varlan, A.1    Hillebrand, M.2
  • 15
    • 46749095895 scopus 로고    scopus 로고
    • Probing midazolam interaction with human serum albumin and its effect on structural state of proteins
    • S.N. Khan, B. Islam, and A.U. Khan Probing midazolam interaction with human serum albumin and its effect on structural state of proteins Int. J. Integrat. Biol. 1 2007 102 112
    • (2007) Int. J. Integrat. Biol. , vol.1 , pp. 102-112
    • Khan, S.N.1    Islam, B.2    Khan, A.U.3
  • 17
    • 58049099712 scopus 로고    scopus 로고
    • Study of the interaction between methyl blue and human serum albumin by fluorescence spectrometry
    • S. Song, X. Hou, Y. Wu, S. Shuang, C. Yang, Y. Inoue, and C. Dong Study of the interaction between methyl blue and human serum albumin by fluorescence spectrometry J. Lumin. 129 2009 169 175
    • (2009) J. Lumin. , vol.129 , pp. 169-175
    • Song, S.1    Hou, X.2    Wu, Y.3    Shuang, S.4    Yang, C.5    Inoue, Y.6    Dong, C.7
  • 18
    • 34247399095 scopus 로고    scopus 로고
    • Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study
    • DOI 10.1016/j.jlumin.2006.06.013, PII S002223130600514X
    • Y.-Q. Wang, H.-M. Zhang, G.-Ch. Zhang, W.-U. Tao, and S.He Tang Interaction of the flavonoid hesperidin with bovine serum albumin. A fluorescence quenching study J. Lumin. 126 2007 211 218 (Pubitemid 46629178)
    • (2007) Journal of Luminescence , vol.126 , Issue.1 , pp. 211-218
    • Wang, Y.-Q.1    Zhang, H.-M.2    Zhang, G.-C.3    Tao, W.-H.4    Tang, S.-H.5
  • 19
    • 0642316329 scopus 로고    scopus 로고
    • Interaction of magnolol with bovine serum albumin: A fluorescence- quenching study
    • DOI 10.1007/s00216-003-2017-8
    • J. Liu, J. Tian, J. Tian, Z. Zhang, and X. Chen Interaction of magnolol with bovine serum albumin: a fluorescence quenching study Anal. Bioanal. Chem. 376 2003 864 867 (Pubitemid 40877950)
    • (2003) Analytical and Bioanalytical Chemistry , vol.376 , Issue.6 , pp. 864-867
    • Liu, J.1    Tian, J.-N.2    Zhang, J.3    Hu, Z.4    Chen, X.5
  • 20
    • 84155171000 scopus 로고    scopus 로고
    • Analysis of binding interaction between Captopril and human serum albumin
    • X. Gao, Y. Tag, W. Rong, X. Zhang, W. Zhao, and Y. Zi Analysis of binding interaction between Captopril and human serum albumin Am. J. Anal. Chem. 2 2011 250 257
    • (2011) Am. J. Anal. Chem. , vol.2 , pp. 250-257
    • Gao, X.1    Tag, Y.2    Rong, W.3    Zhang, X.4    Zhao, W.5    Zi, Y.6
  • 21
    • 52649098026 scopus 로고    scopus 로고
    • Reversible binding of antidiabetic drugs, repaglinide and glicazide, with human serum albumin
    • N. Seedher, and M. Kanojia Reversible binding of antidiabetic drugs, repaglinide and glicazide, with human serum albumin Chem. Biol. Drug. Des. 72 2008 290 296
    • (2008) Chem. Biol. Drug. Des. , vol.72 , pp. 290-296
    • Seedher, N.1    Kanojia, M.2
  • 22
    • 63149160526 scopus 로고    scopus 로고
    • Paclitaxel-albumin interaction in view of molecular engineering of polymer-drug conjugates
    • M. Hess, B.-W. Jo, and S. Wunderlich Paclitaxel-albumin interaction in view of molecular engineering of polymer-drug conjugates Pure Appl. Chem. 81 2009 439 450
    • (2009) Pure Appl. Chem. , vol.81 , pp. 439-450
    • Hess, M.1    Jo, B.-W.2    Wunderlich, S.3
  • 23
    • 0000123455 scopus 로고    scopus 로고
    • Fluorometric determination of drug-protein association constants. The binding of 8-anilino-1-naphthalenesulfonate by bovine serum albumin
    • D.V. Nalk, W.L. Paul, R.M. Threatte, S.J. Schulman, Fluorometric determination of drug-protein association constants. The binding of 8-anilino-1-naphthalenesulfonate by bovine serum albumin, Anal. Chem. 47 (l975) 267-270.
    • Anal. Chem. , vol.47 , Issue.L975 , pp. 267-270
    • Nalk, D.V.1    Paul, W.L.2    Threatte, R.M.3    Schulman, S.J.4
  • 24
    • 0028237710 scopus 로고
    • 2+ antagonist, to serum albumin: A fluorescence study
    • DOI 10.1002/jps.2600830516
    • P. Chatelain, J.-R. Matteazzi, and R. Laurel Binding of fantofarone, a novel Ca(II) antagonist to serum albumin. A fluorescence study J. Pharm. Sci. 83 1994 674 676 (Pubitemid 24219818)
    • (1994) Journal of Pharmaceutical Sciences , vol.83 , Issue.5 , pp. 674-676
    • Chatelain, P.1    Matteazzi, J.-R.2    Laruel, R.3
  • 25
    • 34447556028 scopus 로고    scopus 로고
    • Binding of bioactive phytochemical piperine with human serum albumin: A spectrofluorometric study
    • DOI 10.1002/bip.20735
    • D.V. Suresh, H.G. Mahesha, A.G. Appu Rao, and K. Srinivasan Binding of bioactive phytochemical piperine with human serum albumin: a spectrofluorometric study Biopolymers 86 2007 265 275 (Pubitemid 47067543)
    • (2007) Biopolymers , vol.86 , Issue.4 , pp. 265-275
    • Suresh, D.V.1    Mahesha, H.G.2    Rao, A.G.A.3    Srinivasan, K.4
  • 26
    • 38149080512 scopus 로고    scopus 로고
    • Interaction of 7-hydroxyflavone with human serum albumin: A spectroscopic study
    • A. Banerjee, K. Basu, and P.K. Sengupta Interaction of 7-hydroxyflavone with human serum albumin: a spectroscopic study J. Photochem. Photobiol. B: Biol. 90 2008 33 40
    • (2008) J. Photochem. Photobiol. B: Biol. , vol.90 , pp. 33-40
    • Banerjee, A.1    Basu, K.2    Sengupta, P.K.3
  • 27
    • 77951804336 scopus 로고    scopus 로고
    • Probing the binding interaction of a phenazinium dye with serum transport proteins: A combined fluorometric and circular dichroism study
    • D. Bose, D. Sarkar, and N. Chattophadhyay Probing the binding interaction of a phenazinium dye with serum transport proteins: a combined fluorometric and circular dichroism study Photochem. Photobiol. 86 2010 538 544
    • (2010) Photochem. Photobiol. , vol.86 , pp. 538-544
    • Bose, D.1    Sarkar, D.2    Chattophadhyay, N.3
  • 28
    • 33746190548 scopus 로고
    • A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons
    • H. Benesi, and J. Hildebrand A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons J. Am. Chem. Soc. 71 1949 2703 2707
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 2703-2707
    • Benesi, H.1    Hildebrand, J.2
  • 30
  • 31
    • 0019178958 scopus 로고
    • The interaction of human serum albumin and hemopexin with porphyrins
    • W.T. Morgan, A. Smith, and P. Koskello The interaction of human serum albumin and hemopexin with porphyrins BBA 624 1980 271 285 (Pubitemid 11245029)
    • (1980) Biochimica et Biophysica Acta , vol.624 , Issue.1 , pp. 271-285
    • Morgan, W.T.1    Smith, A.2    Koskelo, P.3
  • 32
    • 52949134053 scopus 로고    scopus 로고
    • Investigation of the interaction between sophoricoside and human serum albumin by optical spectroscopy and molecular modelling methods
    • J. Tang, N. Lian, X. He, and G. Zhang Investigation of the interaction between sophoricoside and human serum albumin by optical spectroscopy and molecular modelling methods J. Mol. Struct. 889 2008 408 414
    • (2008) J. Mol. Struct. , vol.889 , pp. 408-414
    • Tang, J.1    Lian, N.2    He, X.3    Zhang, G.4
  • 33
    • 0013471242 scopus 로고
    • How to illustrate ligand-protein binding in a class experiment
    • A. Marty, M. Boiret, and D. Deumié How to illustrate ligand-protein binding in a class experiment J. Chem. Ed. 63 1986 365 366
    • (1986) J. Chem. Ed. , vol.63 , pp. 365-366
    • Marty, A.1    Boiret, M.2    Deumié, D.3
  • 34
    • 0033228723 scopus 로고    scopus 로고
    • Interaction of acrylodan with human serum albumin. A fluorescence spectroscopic study
    • F. Moreno, M. Cortijo, and J. González-Jiménez Interaction of acrylodan with human serum albumin. A fluorescence spectroscopic study Photochem. Photobiol. 70 1999 695 700 (Pubitemid 129555001)
    • (1999) Photochemistry and Photobiology , vol.70 , Issue.5 , pp. 695-700
    • Moreno, F.1    Cortijo, M.2    Gonzalez-Jimenez, J.3
  • 35
    • 0018387479 scopus 로고
    • Glucocorticoid-mediated alteration in growth factor binding and action. Analysis of the binding change
    • J. Baker, and D.D. Cunningham Glucocorticoid-mediated alteration in growth factor binding and action. Analysis of the binding change J. Supramol. Struct. 9 1978 69 77
    • (1978) J. Supramol. Struct. , vol.9 , pp. 69-77
    • Baker, J.1    Cunningham, D.D.2
  • 36
    • 0028989459 scopus 로고
    • A general, wide-range, spectrofluorimetric method for measuring the site-specific affinities of drugs towards human serum albumin
    • D.E. Epps, T.J. Raub, and F.J. Kezdy A general, wide-range, spectrofluorimetric method for measuring the site-specific affinities of drugs towards human serum albumin Anal. Biochem. 227 1995 342 350
    • (1995) Anal. Biochem. , vol.227 , pp. 342-350
    • Epps, D.E.1    Raub, T.J.2    Kezdy, F.J.3
  • 37
    • 62349099551 scopus 로고    scopus 로고
    • Fluorescence study of site-specific binding of perfluoroalkyl acids to human serum albumin
    • Y.-M. Chen, and L.-H. Guo Fluorescence study of site-specific binding of perfluoroalkyl acids to human serum albumin Arch. Toxicol. 83 2009 255 261
    • (2009) Arch. Toxicol. , vol.83 , pp. 255-261
    • Chen, Y.-M.1    Guo, L.-H.2
  • 38
    • 59449101840 scopus 로고    scopus 로고
    • Binding properties of hydrophobic molecules to human serum albumin studied by fluorescence titration
    • K. Takehara, K. Yuki, M. Shirasawa, S. Yamasaki, and S. Yamada Binding properties of hydrophobic molecules to human serum albumin studied by fluorescence titration Anal. Sci. 25 2009 115 120
    • (2009) Anal. Sci. , vol.25 , pp. 115-120
    • Takehara, K.1    Yuki, K.2    Shirasawa, M.3    Yamasaki, S.4    Yamada, S.5
  • 39
    • 61949432567 scopus 로고    scopus 로고
    • Structural analysis of human serum albumin with cationic lipids
    • D. Charbonneau, M. Beauregard, and H.-A. Tajmir-Riahi Structural analysis of human serum albumin with cationic lipids J. Phys. Chem. B 113 2009 1777 1784
    • (2009) J. Phys. Chem. B , vol.113 , pp. 1777-1784
    • Charbonneau, D.1    Beauregard, M.2    Tajmir-Riahi, H.-A.3
  • 41
    • 3242709482 scopus 로고    scopus 로고
    • Investigation of the interaction between flavonoids and human serum albumin
    • DOI 10.1016/j.molstruc.2004.05.026, PII S0022286004004223
    • S. Bi, L. Ding, Y. Tian, D. Song, X. Zghou, X. Liu, and H. Zhang Investigation of the interaction between flavonoids and human serum albumin J. Mol. Struct. 73 2004 37 45 (Pubitemid 38953410)
    • (2004) Journal of Molecular Structure , vol.703 , Issue.1-3 , pp. 37-45
    • Bi, S.1    Ding, L.2    Tian, Y.3    Song, D.4    Zhou, X.5    Liu, X.6    Zhang, H.7
  • 42
    • 79955640298 scopus 로고    scopus 로고
    • Protaein-binding and antioxidant potential of phenolics of mangosteen fruit (Garcinia mangostana)
    • M. Naczk, M. Towsend, R. Zadernowski, and F. Shahidi Protaein-binding and antioxidant potential of phenolics of mangosteen fruit (Garcinia mangostana) Food Chem. 128 2011 292 298
    • (2011) Food Chem. , vol.128 , pp. 292-298
    • Naczk, M.1    Towsend, M.2    Zadernowski, R.3    Shahidi, F.4
  • 43
    • 66349101345 scopus 로고    scopus 로고
    • Spectroscopic investigations of the binding interaction of a new indanedione derivative with human and bovine serum albumins
    • D. Stan, I. Matei, C. Mihailescu, M. Savin, M. Matache, M. Hillebrand, and I. Baciu Spectroscopic investigations of the binding interaction of a new indanedione derivative with human and bovine serum albumins Molecules 14 2009 1614 1626
    • (2009) Molecules , vol.14 , pp. 1614-1626
    • Stan, D.1    Matei, I.2    Mihailescu, C.3    Savin, M.4    Matache, M.5    Hillebrand, M.6    Baciu, I.7
  • 44
    • 77956962964 scopus 로고    scopus 로고
    • The interaction of lysozyme with caffeine, theophyline and theobromine in solution
    • H.-M. Zhang, B.-P. Tang, and Y.-Q. Wang The interaction of lysozyme with caffeine, theophyline and theobromine in solution Mol. Biol. Rep. 37 2010 3127 3136
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 3127-3136
    • Zhang, H.-M.1    Tang, B.-P.2    Wang, Y.-Q.3
  • 47
    • 49449116404 scopus 로고    scopus 로고
    • Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes
    • O.K. Abou-Zied, and O.I.K. Al-Shihi Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes J. Am. Chem. Soc. 130 2008 10793 10801
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10793-10801
    • Abou-Zied, O.K.1    Al-Shihi, O.I.K.2
  • 48
    • 34248230854 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from tryptophan in human serum albumin to a bioactive indoloquinolizine system
    • DOI 10.1007/s12039-007-0013-9
    • P. Das, A. Mallick, B. Haldar, A. Chakrabarty, and N. Chattopadhyay Fluorescence resonance energy transfer from tryptophan in human serum albumin to a bioactive indoloquinolizine system J. Chem. Sci. 119 2007 77 82 (Pubitemid 46715188)
    • (2007) Journal of Chemical Sciences , vol.119 , Issue.2 , pp. 77-82
    • Das, P.1    Mallick, A.2    Haldar, B.3    Chakrabarty, A.4    Chattopadhyay, N.5
  • 49
    • 0014199062 scopus 로고
    • The binding of oligosacharides containing N-acetylglucosamine and N-acetylmuramic acid to lysozyme
    • D.M. Chipman, V. Grisaro, and N. Sharon The binding of oligosacharides containing N-acetylglucosamine and N-acetylmuramic acid to lysozyme J. Biol. Chem. 242 1967 4388 4394
    • (1967) J. Biol. Chem. , vol.242 , pp. 4388-4394
    • Chipman, D.M.1    Grisaro, V.2    Sharon, N.3
  • 50
    • 80052970305 scopus 로고    scopus 로고
    • On the evaluation of the number of binding sites in proteins from steady state fluorescence measurements
    • E. Lissi, and E. Abuin On the evaluation of the number of binding sites in proteins from steady state fluorescence measurements J. Fluoresc. 21 2011 1831 1833
    • (2011) J. Fluoresc. , vol.21 , pp. 1831-1833
    • Lissi, E.1    Abuin, E.2
  • 51
    • 77950865952 scopus 로고    scopus 로고
    • Fluorescence quenching to study protein-ligand binding: Common errors
    • M. van de Weert Fluorescence quenching to study protein-ligand binding: common errors Fluorescence 20 2010 625 629
    • (2010) Fluorescence , vol.20 , pp. 625-629
    • Van De Weert, M.1
  • 52
    • 0000672238 scopus 로고
    • The association of imidazole with the ions of Zinc and Cupric Copper
    • J.T. Edsall, G. Felsenfeld, D.S. Goodman, and F.R.N. Gurd The association of imidazole with the ions of Zinc and Cupric Copper J. Am. Chem. Soc 76 1954 3054 3058
    • (1954) J. Am. Chem. Soc , vol.76 , pp. 3054-3058
    • Edsall, J.T.1    Felsenfeld, G.2    Goodman, D.S.3    Gurd, F.R.N.4
  • 53
    • 34249693111 scopus 로고    scopus 로고
    • Spectroscopic investigation on the interaction of J-aggregate with human serum albumin
    • DOI 10.1016/j.bpc.2007.04.002, PII S0301462207000841
    • Y. Zhang, H. Du, Y. Tang, G. Xu, and W. Yang Spectroscopic investigation of the interaction of J-aggregates with human serum albumin Biophys. Chem. 128 2007 197 203 (Pubitemid 46843443)
    • (2007) Biophysical Chemistry , vol.128 , Issue.2-3 , pp. 197-203
    • Zhang, Y.1    Du, H.2    Tang, Y.3    Xu, G.4    Yan, W.5
  • 54
    • 1042302180 scopus 로고    scopus 로고
    • Complexation of polymethine dyes with human serum albumin: A spectroscopic study
    • DOI 10.1016/S0301-4622(03)00218-7
    • A.S. Tatikolov, and S.M.B. Costa Complexation of polymethine dyes with human serum albumin: a spectroscopy study Biophys. Chem. 107 2004 33 49 (Pubitemid 38197980)
    • (2004) Biophysical Chemistry , vol.107 , Issue.1 , pp. 33-49
    • Tatikolov, A.S.1    Costa, S.M.B.2
  • 57
    • 0024583031 scopus 로고
    • Evidence for isoxicam binding to site I as a primary site and to site II as a secondary site of human serum albumin
    • DOI 10.1016/0006-2952(89)90227-X
    • F. Bree, P. Nguyen, E. Albengres, S. Urien, P. Riant, P.G. Welling, and J.-P. Tillement Evidence for isoxicam binding to Site I as a primary site and to Site II as a secondary site of human serum albumin Biochem. Pharmacol. 38 1989 753 758 (Pubitemid 19072675)
    • (1989) Biochemical Pharmacology , vol.38 , Issue.5 , pp. 753-758
    • Bree, F.1    Nguyen, P.2    Albengres, E.3    Urien, S.4    Riant, P.5    Welling, P.G.6    Tillement, J.-P.7
  • 58
    • 0037051853 scopus 로고    scopus 로고
    • Effects of photoproducts on the binding properties of protoporphyrin IX to proteins
    • DOI 10.1016/S0301-4622(02)00035-2, PII S0301462202000352
    • L. Brancaleon, and H. Moseley Effects of photoproducts on the binding properties of protoporphyrin IX to proteins Biophys. Chem. 96 2002 77 87 (Pubitemid 34303303)
    • (2002) Biophysical Chemistry , vol.96 , Issue.1 , pp. 77-87
    • Brancaleon, L.1    Moseley, H.2
  • 59
    • 0019331899 scopus 로고
    • Inverse dependence of binding constant upon albumin concentration. Results for l-tryptophan and three anionic dyes
    • C.J. Bowmer, and W.E. Lindup Inverse dependence of binding constant upon albumin concentration. Results for l-tryptophan and three anionic dyes BBA 624 1980 260 270
    • (1980) BBA , vol.624 , pp. 260-270
    • Bowmer, C.J.1    Lindup, W.E.2
  • 60
    • 49049139427 scopus 로고
    • Evaluation of partition constants in compartimentalised systems from fluorescence quenching data
    • M.V. Encinas, and E. Lissi Evaluation of partition constants in compartimentalised systems from fluorescence quenching data Chem. Phys. Lett. 91 1982 55 57
    • (1982) Chem. Phys. Lett. , vol.91 , pp. 55-57
    • Encinas, M.V.1    Lissi, E.2
  • 61
    • 0037016359 scopus 로고    scopus 로고
    • A new and simple procedure for the evaluation of the association of surfactants to proteins
    • DOI 10.1016/S0165-022X(01)00237-8, PII S0165022X01002378
    • E. Lissi, E. Abuin, M.E. Lanio, and C. Alvarez A new and simple procedure for the evaluation of the association of surfactants to proteins J. Biochim. Biophys. Methods 50 2002 261 268 (Pubitemid 34015924)
    • (2002) Journal of Biochemical and Biophysical Methods , vol.50 , Issue.2-3 , pp. 261-268
    • Lissi, E.1    Abuin, E.2    Lanio, M.E.3    Alvarez, C.4
  • 62
    • 0037456021 scopus 로고    scopus 로고
    • Quenching of BSA intrinsic fluorescence by alkylpyridinium cations. Its relationship to surfactant-protein association
    • PII S1010603002003556
    • X. Diaz, E. Abuin, and E. Lissi Quenching of BSA intrinsic fluorescence by alkylpyridinium cations. Its relationship to surfactant-protein association J. Photochem. Photobiol. A. Chem. 155 2003 157 162 (Pubitemid 36196820)
    • (2003) Journal of Photochemistry and Photobiology A: Chemistry , vol.155 , Issue.1-3 , pp. 157-162
    • Diaz, X.1    Abuin, E.2    Lissi, E.3
  • 63
    • 0022542006 scopus 로고
    • The association of acrylamide with proteins. The interpretation of fluorescence quenching experiments
    • E. Blatt, A. Husain, and W.H. Sawyer The association of acrylamide with proteins. The interpretation of fluorescence quenching experiments BBA 871 1986 613
    • (1986) BBA , vol.871 , pp. 613
    • Blatt, E.1    Husain, A.2    Sawyer, W.H.3
  • 64
    • 33644533548 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer and molecular modelling studies on 4′6-diamidino-2-phenylindole (DAPI) complexes with tubulin
    • J.J. Arbildua, J. Brunet, D.M. Jameson, M. Lopez, E. Nova, R. Lagos, and O. Monasterio Fluorescence resonance energy transfer and molecular modelling studies on 4′6-diamidino-2-phenylindole (DAPI) complexes with tubulin Protein Sci. 15 2006 410 419
    • (2006) Protein Sci. , vol.15 , pp. 410-419
    • Arbildua, J.J.1    Brunet, J.2    Jameson, D.M.3    Lopez, M.4    Nova, E.5    Lagos, R.6    Monasterio, O.7
  • 65
    • 40849121069 scopus 로고    scopus 로고
    • Resonance energy transfer and ligand binding studies on pH-induced folded states of human serum albumin
    • DOI 10.1016/j.jphotobiol.2008.01.001, PII S1011134408000031
    • A.K. Shaw, and S.K. Pal Resonance energy transfer and ligand binding studies on pH induced folded states of human serum albumin J. Photochem. Photobiol. B: Biol. 90 2008 187 197 (Pubitemid 351391676)
    • (2008) Journal of Photochemistry and Photobiology B: Biology , vol.90 , Issue.3 , pp. 187-197
    • Shaw, A.K.1    Pal, S.K.2
  • 66
    • 0015239160 scopus 로고
    • Fluorescence of glycogen phosphorylase b. Structural transitions and energy transfer
    • M. Cortijo, I.Z. Steinberg, and S. Shaltiel Fluorescence of glycogen phosphorylase b. Structural transitions and energy transfer J. Biol. Chem. 246 1971 933 938
    • (1971) J. Biol. Chem. , vol.246 , pp. 933-938
    • Cortijo, M.1    Steinberg, I.Z.2    Shaltiel, S.3
  • 67
    • 77951093406 scopus 로고    scopus 로고
    • Misconceptions over Forster resonance energy transfer between proteins and ANS/bis-ANS: Direct excitation dominates dye fluorescence
    • A. Hawe, R. Poole, and W. Jiskoot Misconceptions over Forster resonance energy transfer between proteins and ANS/bis-ANS: direct excitation dominates dye fluorescence Anal. Biochem. 401 2010 99 106
    • (2010) Anal. Biochem. , vol.401 , pp. 99-106
    • Hawe, A.1    Poole, R.2    Jiskoot, W.3
  • 68
    • 79954623277 scopus 로고    scopus 로고
    • Simultaneous binding of anti-tuberculosis and anti-thrombosis drugs to a human transporter protein: A FRET study
    • P. Rajdev, T. Mondol, A. Makhal, and S.K. Pal Simultaneous binding of anti-tuberculosis and anti-thrombosis drugs to a human transporter protein: a FRET study J. Photochem. Photobiol. B: Biol. 103 2011 153 158
    • (2011) J. Photochem. Photobiol. B: Biol. , vol.103 , pp. 153-158
    • Rajdev, P.1    Mondol, T.2    Makhal, A.3    Pal, S.K.4
  • 69
    • 0028863648 scopus 로고
    • The effects of aggregation, protein binding and cellular incorporation on the photophysical properties of benzoporphyrin derivative monoacid ring A (BPDMA)
    • B.M. Avelline, T. Hassan, and R.W. Redmond The effects of aggregation, protein binding and cellular incorporation on the photophysical properties of benzoporphyrin derivative monoacid ring A (BPDMA) J. Photochem. Photobiol. B: Biol. 30 1995 161 169
    • (1995) J. Photochem. Photobiol. B: Biol. , vol.30 , pp. 161-169
    • Avelline, B.M.1    Hassan, T.2    Redmond, R.W.3
  • 70
    • 0642309823 scopus 로고    scopus 로고
    • Fluorescence studies on the interactions of barbaloin with bovine serum albumin
    • J. Tian, J. Liu, J. Zhang, Z. Hu, and X. Chen Fluorescence studies on the interactions of barbaloin with bovine serum albumin Chem. Pharm. Bull. 51 2003 579 582 (Pubitemid 41656811)
    • (2003) Chemical and Pharmaceutical Bulletin , vol.51 , Issue.5 , pp. 579-582
    • Tian, J.1    Liu, J.2    Zhang, J.3    Hu, Z.4    Chen, X.5
  • 71
    • 0006579432 scopus 로고    scopus 로고
    • Interaction of curcumin with human serum albumin - A spectroscopic study
    • A.Ch. Pulla Reddy, E. Sudharshan, A.G. Appu Rao, and B.R. Lokesh Interaction of curcumin with human serum albumin - a spectroscopic study Lipids 34 1999 1025 1028
    • (1999) Lipids , vol.34 , pp. 1025-1028
    • Pulla Reddy, A.Ch.1    Sudharshan, E.2    Appu Rao, A.G.3    Lokesh, B.R.4
  • 72
    • 67650391671 scopus 로고    scopus 로고
    • Investigation of the interaction between pentachlorophenol and human serum albumin using spectral methods
    • Y.-Q. Wang, H.-M. Zhang, and Q.-H. Zhou Investigation of the interaction between pentachlorophenol and human serum albumin using spectral methods J. Mol. Struct. 932 2009 3137
    • (2009) J. Mol. Struct. , vol.932 , pp. 3137
    • Wang, Y.-Q.1    Zhang, H.-M.2    Zhou, Q.-H.3
  • 73
    • 0023235043 scopus 로고
    • Fluorescence energy transfer study of the relationship between the lone tryptophan residue and drug binding sites in human serum albumin
    • S. Kasai, T. Horie, T. Mizuma, and S. Awazu Fluorescence energy transfer study of the relationship between the lone tryptophan residue and drug binding sites in human serum albumin J. Pharm. Sci. 76 1967 387 392
    • (1967) J. Pharm. Sci. , vol.76 , pp. 387-392
    • Kasai, S.1    Horie, T.2    Mizuma, T.3    Awazu, S.4
  • 74
    • 33646237433 scopus 로고    scopus 로고
    • Interaction of surface-active fluorescence probes with bovine serum albumin
    • T.K. Xu, X.S. Shen, N. Li, and H.C. Gao Interaction of surface-active fluorescence probes with bovine serum albumin Chin. Chem. Lett. 16 2005 943 946 (Pubitemid 43872271)
    • (2005) Chinese Chemical Letters , vol.16 , Issue.7 , pp. 943-946
    • Xu, T.K.1    Shen, X.H.2    Li, N.3    Gao, H.C.4
  • 75
    • 70349099296 scopus 로고    scopus 로고
    • Binding of the scutellarin to albumin using tryptophan fluorescence quenching, CD and FT-IR spectra
    • F. Tian, J. Liu, Z. Hu, and X. Chen Binding of the scutellarin to albumin using tryptophan fluorescence quenching, CD and FT-IR spectra Am. J. Immunol. 1 2005 21 23
    • (2005) Am. J. Immunol. , vol.1 , pp. 21-23
    • Tian, F.1    Liu, J.2    Hu, Z.3    Chen, X.4
  • 76
    • 33749319756 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between riboflavin and albumins
    • Z. Hongwei, G. Min, Z. Zhaoxia, W. Wenfeng, and W. Guozhong Spectroscopic studies on the interaction between riboflavin and albumins Spectrochim. Acta A 65 2006 811 817
    • (2006) Spectrochim. Acta A , vol.65 , pp. 811-817
    • Hongwei, Z.1    Min, G.2    Zhaoxia, Z.3    Wenfeng, W.4    Guozhong, W.5
  • 77
    • 34548152571 scopus 로고    scopus 로고
    • Nitroaniline isomers interaction with bovine serum albumin and toxicological implications
    • DOI 10.1007/s10895-007-0203-3
    • G. Xiang, C. Tong, and H. Lin Nitroaniline isomers interaction with bovine serum albumin and toxicological implications J. Fluoresc. 17 2007 512 521 (Pubitemid 47310323)
    • (2007) Journal of Fluorescence , vol.17 , Issue.5 , pp. 512-521
    • Xiang, G.1    Tong, C.2    Lin, H.3
  • 78
    • 4444325241 scopus 로고    scopus 로고
    • The study of the interaction between human serum albumin and a new reagent with antitumor activity by spectrophotometric methods
    • H. Gao, L. Lei, J. Liu, Q. Kong, X. Chen, and Z. Hu The study of the interaction between human serum albumin and a new reagent with antitumor activity by spectrophotometric methods J. Photochem. Photobiol. A: Chem. 167 2004 213 221
    • (2004) J. Photochem. Photobiol. A: Chem. , vol.167 , pp. 213-221
    • Gao, H.1    Lei, L.2    Liu, J.3    Kong, Q.4    Chen, X.5    Hu, Z.6
  • 79
    • 26644456682 scopus 로고    scopus 로고
    • Study of the interaction between fluoroquinolones and bovine serum albumin
    • DOI 10.1016/j.jpba.2005.05.013, PII S0731708505003559
    • B.P. Kamat Study on the interaction between fluoroquinolones and bovine serum albumin J. Pharm. Biomed. Anal. 39 2005 1046 1050 (Pubitemid 41441736)
    • (2005) Journal of Pharmaceutical and Biomedical Analysis , vol.39 , Issue.5 , pp. 1046-1050
    • Kamat, B.P.1
  • 81
    • 35348971410 scopus 로고    scopus 로고
    • Probing the interaction of ellagic acid with human serum albumin: A fluorescence spectroscopic study
    • R.K. Nanda, N. Sarkar, and R. Banerjee Probing the interaction of ellagic acid with human serum albumin: a fluorescence spectroscopic study J. Photochem. Photobiol. A: Chem. 192 2007 152 158
    • (2007) J. Photochem. Photobiol. A: Chem. , vol.192 , pp. 152-158
    • Nanda, R.K.1    Sarkar, N.2    Banerjee, R.3
  • 82
    • 21744445084 scopus 로고    scopus 로고
    • A molecular dynamics study of human serum albumin binding sites
    • DOI 10.1016/j.farmac.2005.04.010, PII S0014827X0500087X
    • R. Artali, G. Bombieri, L. Calabi, and A. Del Pra A molecular dynamic study of human serum albumin binding sites Il Farmaco 60 2005 485 495 (Pubitemid 40943387)
    • (2005) Farmaco , vol.60 , Issue.6-7 , pp. 485-495
    • Artali, R.1    Bombieri, G.2    Calabi, L.3    Del Pra, A.4
  • 84
    • 55949121032 scopus 로고    scopus 로고
    • Interaction of mitoxantrone with human serum albumin: Spectroscopic and molecular modelling studies
    • S.N. Khan, B. Islam, R. Yennamalli, A. Sultan, N. Subbarao, and A.U. Khan Interaction of mitoxantrone with human serum albumin: spectroscopic and molecular modelling studies Eur. J. Pharm. Sci. 35 2008 371 372
    • (2008) Eur. J. Pharm. Sci. , vol.35 , pp. 371-372
    • Khan, S.N.1    Islam, B.2    Yennamalli, R.3    Sultan, A.4    Subbarao, N.5    Khan, A.U.6
  • 85
    • 39749120538 scopus 로고    scopus 로고
    • Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin
    • F. Wang, W. Huang, and Z. Dai Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin J. Mol. Struct. 875 2008 59 514
    • (2008) J. Mol. Struct. , vol.875 , pp. 59-514
    • Wang, F.1    Huang, W.2    Dai, Z.3
  • 86
    • 84155162705 scopus 로고    scopus 로고
    • A spectroscopy study of the interaction of the antioxidant naringin with bovine serum albumin
    • A.S. Roy, D.R. Tripathy, A. Chatterjee, and S. Dasgupta A spectroscopy study of the interaction of the antioxidant naringin with bovine serum albumin J. Biophys. Chem. 1 2010 141 152
    • (2010) J. Biophys. Chem. , vol.1 , pp. 141-152
    • Roy, A.S.1    Tripathy, D.R.2    Chatterjee, A.3    Dasgupta, S.4
  • 88
    • 7244247482 scopus 로고    scopus 로고
    • Concerning the photodiastereomerization and protic equilibria of urocanic acid and its complex with human serum albumin
    • DOI 10.1007/s00706-004-0219-1
    • B. Schwarzinger, and H. Falk Concerning the photodiastereomerization and protic equilibria of urocanic acid and its complex with human serum albumin Monatsh. Chem. 135 2004 1297 1304 (Pubitemid 39429406)
    • (2004) Monatshefte fur Chemie , vol.135 , Issue.10 , pp. 1297-1304
    • Schwarzinger, B.1    Falk, H.2
  • 89
    • 44749093227 scopus 로고    scopus 로고
    • Spectroscopic investigation on the binding of bioactive pyridazinone derivative to human serum albumin and molecular modelling
    • T. Wang, B. Xiang, Y. Wan, C. Chen, Y. Dong, H. Fang, and M. Wang Spectroscopic investigation on the binding of bioactive pyridazinone derivative to human serum albumin and molecular modelling Coll. Surf. B: Biointerf. 65 2008 113 119
    • (2008) Coll. Surf. B: Biointerf. , vol.65 , pp. 113-119
    • Wang, T.1    Xiang, B.2    Wan, Y.3    Chen, C.4    Dong, Y.5    Fang, H.6    Wang, M.7
  • 90
    • 34548258775 scopus 로고    scopus 로고
    • Study of interaction between apigenin and human serum albumin by spectroscopy and molecular modelling
    • J.-L. Yuan, L.V. Zhong, Z.-G. Liu, Z. Hu, and G.-L. Zou Study of interaction between apigenin and human serum albumin by spectroscopy and molecular modelling J. Photochem. Photobiol. A: Chem. 191 2007 104 113
    • (2007) J. Photochem. Photobiol. A: Chem. , vol.191 , pp. 104-113
    • Yuan, J.-L.1    Zhong, L.V.2    Liu, Z.-G.3    Hu, Z.4    Zou, G.-L.5
  • 91
    • 34249808535 scopus 로고    scopus 로고
    • Interaction of tetrandrine with human serum albumin: A fluorescence quenching study
    • C. Wang, U.-H. Wu, C.-R. Li, Z. Wang, J.-J. Ma, X.-H. Zang, and N.-X. Qin Interaction of tetrandrine with human serum albumin: a fluorescence quenching study Anal. Sci. 23 2007 429 433
    • (2007) Anal. Sci. , vol.23 , pp. 429-433
    • Wang, C.1    Wu, U.-H.2    Li, C.-R.3    Wang, Z.4    Ma, J.-J.5    Zang, X.-H.6    Qin, N.-X.7
  • 92
    • 77955421042 scopus 로고    scopus 로고
    • Binding of several benzodiazepines to bovine serum albumin. Fluorescence study
    • R.G. Machicote, M.E. Pacheco, and L. Bruzzone Binding of several benzodiazepines to bovine serum albumin. Fluorescence study Spectrochim. Acta A 77 2010 466 472
    • (2010) Spectrochim. Acta A , vol.77 , pp. 466-472
    • MacHicote, R.G.1    Pacheco, M.E.2    Bruzzone, L.3
  • 93
    • 76349087824 scopus 로고    scopus 로고
    • Identification of pyrazosulfuron-ethyl binding affinity and binding site subdomain IIA in human serum albumin by spectroscopic methods
    • F. Ding, W. Liu, X. Zhang, Wu. L-J, L. Zhang, and Y. Sun Identification of pyrazosulfuron-ethyl binding affinity and binding site subdomain IIA in human serum albumin by spectroscopic methods Spectrochim. Acta A 75 2010 1088 1094
    • (2010) Spectrochim. Acta A , vol.75 , pp. 1088-1094
    • Ding, F.1    Liu, W.2    Zhang, X.3    Wu, L.-J.4    Zhang, L.5    Sun, Y.6
  • 94
    • 70349144035 scopus 로고    scopus 로고
    • The effect of methylamine on the solution structures of human and bovine serum albumins
    • S. Hamdani, D. Joly, R. Carpentier, and H.A. Tajmir-Riahi The effect of methylamine on the solution structures of human and bovine serum albumins J. Mol. Struct. 936 2009 80 85
    • (2009) J. Mol. Struct. , vol.936 , pp. 80-85
    • Hamdani, S.1    Joly, D.2    Carpentier, R.3    Tajmir-Riahi, H.A.4
  • 95
    • 70349237017 scopus 로고    scopus 로고
    • Deciphering the fluorescence resonance energy transfer signature of 3-pyrazolyl-2-pyrazoline in transport proteinous environments
    • P. Banerjee, S. Pramanik, A. Sarkar, and S.C. Bhattacharya Deciphering the fluorescence resonance energy transfer signature of 3-pyrazolyl-2-pyrazoline in transport proteinous environments J. Phys. Chem. B 113 2009 11429 11436
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11429-11436
    • Banerjee, P.1    Pramanik, S.2    Sarkar, A.3    Bhattacharya, S.C.4
  • 97
    • 77954864482 scopus 로고    scopus 로고
    • Characterization of interaction and the effect of carbamazepine on the structure of human serum albumin
    • S.S. Kalanur, J. Seetharamappa, and V.K.A. Kalalbandi Characterization of interaction and the effect of carbamazepine on the structure of human serum albumin J. Pharm. Biomed. Anal. 53 2010 660 666
    • (2010) J. Pharm. Biomed. Anal. , vol.53 , pp. 660-666
    • Kalanur, S.S.1    Seetharamappa, J.2    Kalalbandi, V.K.A.3
  • 98
    • 72649100029 scopus 로고    scopus 로고
    • Probing the binding of fluoxetine hydrochloride to human serum albumin by multispectroscopic techniques
    • U. Datrahalli, S. Jaldappagari, and S.S. Kalanur Probing the binding of fluoxetine hydrochloride to human serum albumin by multispectroscopic techniques Spectrochim. Acta A 75 2010 314 319
    • (2010) Spectrochim. Acta A , vol.75 , pp. 314-319
    • Datrahalli, U.1    Jaldappagari, S.2    Kalanur, S.S.3
  • 99
    • 55249121848 scopus 로고    scopus 로고
    • Interaction of the irisflorentin with bovine serum albumin: A fluorescence quenching study
    • G. Zhang, A. Wang, T. Jiang, and J. Guo Interaction of the irisflorentin with bovine serum albumin: a fluorescence quenching study J. Mol. Struct. 891 2008 93 97
    • (2008) J. Mol. Struct. , vol.891 , pp. 93-97
    • Zhang, G.1    Wang, A.2    Jiang, T.3    Guo, J.4
  • 100
    • 78649631183 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer: A promising tool for investigation of the interaction between 1-anthracene sulphonate and serum albumins
    • P. Banerjee, S. Ghosh, A. Sarkar, and S.Ch. Bhattacharya Fluorescence resonance energy transfer: a promising tool for investigation of the interaction between 1-anthracene sulphonate and serum albumins J. Lumin. 131 2011 316 321
    • (2011) J. Lumin. , vol.131 , pp. 316-321
    • Banerjee, P.1    Ghosh, S.2    Sarkar, A.3    Bhattacharya, S.Ch.4
  • 101
    • 71749096547 scopus 로고    scopus 로고
    • Fluorescence resonance energy-transfer affects the determination of the affinity between ligand and proteins obtained by fluorescence quenching method
    • J. Xiao, X. Wei, Y. Wang, and Ch. Liu Fluorescence resonance energy-transfer affects the determination of the affinity between ligand and proteins obtained by fluorescence quenching method Spectrochim. Acta A 74 2009 977 982
    • (2009) Spectrochim. Acta A , vol.74 , pp. 977-982
    • Xiao, J.1    Wei, X.2    Wang, Y.3    Liu, Ch.4
  • 102
    • 70449084682 scopus 로고    scopus 로고
    • Interaction of kaempferol with human serum albumin. A fluorescence and circular dichroism study
    • J. Matei, and M. Hillebrand Interaction of kaempferol with human serum albumin. A fluorescence and circular dichroism study J. Pharm. Biomed. Anal. 51 2010 768 773
    • (2010) J. Pharm. Biomed. Anal. , vol.51 , pp. 768-773
    • Matei, J.1    Hillebrand, M.2
  • 105
  • 106
    • 33744910633 scopus 로고    scopus 로고
    • Interaction of ICT receptor with serum albumins in aqueous buffer
    • DOI 10.1016/j.cplett.2006.05.019, PII S0009261406006646
    • Wu. F-Y, Ji. Z-J, Wu. Y-M, and X.-F. Wan Interaction of ICT receptor with serum albumins in aqueous buffer Chem. Phys. Lett. 424 2006 387 393 (Pubitemid 43850468)
    • (2006) Chemical Physics Letters , vol.424 , Issue.4-6 , pp. 387-393
    • Wu, F.-Y.1    Ji, Z.-J.2    Wu, Y.-M.3    Wan, X.-F.4
  • 108
    • 33750802748 scopus 로고    scopus 로고
    • Human serum albumin interaction with paraquat studied using spectroscopic methods
    • DOI 10.1016/j.pestbp.2006.05.003, PII S0048357506000708
    • G. Zhang, Y. Wang, H. Shang, S. Tang, and W. Tao Human serum albumin interaction with paraquat studied using spectroscopic methods Pesticide Biochem. Physiol. 87 2007 23 29 (Pubitemid 44712013)
    • (2007) Pesticide Biochemistry and Physiology , vol.87 , Issue.1 , pp. 23-29
    • Zhang, G.1    Wang, Y.2    Zhang, H.3    Tang, S.4    Tao, W.5
  • 109
    • 35548983013 scopus 로고    scopus 로고
    • Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and modeling
    • DOI 10.1016/j.molstruc.2007.01.020, PII S0022286007000622
    • D. Li, J. Zhu, J. Jin, and X. Yao Studies on the binding of nevadensin to human serum albumin by molecular spectroscopy and modelling J. Mol. Struct. 846 2007 34 41 (Pubitemid 350016013)
    • (2007) Journal of Molecular Structure , vol.846 , Issue.1-3 , pp. 34-41
    • Li, D.1    Zhu, J.2    Jin, J.3    Yao, X.4
  • 110
  • 111
    • 5044238048 scopus 로고    scopus 로고
    • Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modeling method
    • DOI 10.1021/bm049668m
    • J. Tian, J. Liu, W. He, Z. Hu, X. Yao, and X. Chen Probing the binding of scutellarin to human serum albumin by circular dichroism, fluorescence spectroscopy, FTIR, and molecular modelling method Biomacromolecules 5 2004 1956 1961 (Pubitemid 39335237)
    • (2004) Biomacromolecules , vol.5 , Issue.5 , pp. 1956-1961
    • Tian, J.1    Liu, J.2    He, W.3    Hu, Z.4    Yao, X.5    Chen, X.6
  • 112
    • 53849098410 scopus 로고    scopus 로고
    • Spectroscopic studies on the interaction between nicotinamide and bovine serum albumin
    • H. Xu, Q. Liu, and Y. Wen Spectroscopic studies on the interaction between nicotinamide and bovine serum albumin Spectrochim. Acta A 71 2008 984 988
    • (2008) Spectrochim. Acta A , vol.71 , pp. 984-988
    • Xu, H.1    Liu, Q.2    Wen, Y.3
  • 113
    • 32144451207 scopus 로고    scopus 로고
    • Interaction of m-nitrophenylfluorone-Mo(VI) complex as a probe with human serum albumin: A fluorescence quenching study
    • DOI 10.1016/j.saa.2005.05.040, PII S1386142505002866
    • Q. Wei, D. Wu, B. Du, Y. Li, and C. Duan Interaction of m-nitrophenyl fluorine-Mo (VI) complex as a probe with human serum albumin: a fluorescence quenching study Spectrochim. Acta A 63 2006 532 535 (Pubitemid 43207718)
    • (2006) Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy , vol.63 , Issue.3 , pp. 532-535
    • Wei, Q.1    Wu, D.2    Du, B.3    Li, Y.4    Duan, C.5
  • 114
    • 61449132323 scopus 로고    scopus 로고
    • Characterization of the mangiferin-human serum albumin complex by spectroscopy and molecular modelling approach
    • Y. Yue, X. Chen, J. Qin, and X. Yao Characterization of the mangiferin-human serum albumin complex by spectroscopy and molecular modelling approach J. Pharm. Biomed. Anal. 49 2009 753 759
    • (2009) J. Pharm. Biomed. Anal. , vol.49 , pp. 753-759
    • Yue, Y.1    Chen, X.2    Qin, J.3    Yao, X.4
  • 116
    • 46149110518 scopus 로고    scopus 로고
    • Characterization of interaction between bergenin and human serum albumin in membrane mimetic environments
    • Y. Zhang, L. Dong, Y. Li, J. Li, and Z. Chen Characterization of interaction between bergenin and human serum albumin in membrane mimetic environments J. Fluoresc. 18 2008 661 670
    • (2008) J. Fluoresc. , vol.18 , pp. 661-670
    • Zhang, Y.1    Dong, L.2    Li, Y.3    Li, J.4    Chen, Z.5
  • 117
    • 43449099413 scopus 로고    scopus 로고
    • Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy
    • G. Zhang, Q. Que, J. Pan, and J. Guo Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy J. Mol. Struct. 881 2008 123 138
    • (2008) J. Mol. Struct. , vol.881 , pp. 123-138
    • Zhang, G.1    Que, Q.2    Pan, J.3    Guo, J.4
  • 118
    • 1642317115 scopus 로고    scopus 로고
    • Binding of wogonin to human serum albumin: A common binding site of wogonin in subdomain IIA
    • DOI 10.1016/j.jphotobiol.2004.01.001, PII S101113440400003X
    • J. Tian, J. Liu, J. Xie, X. Yao, Z. Hu, and X. Chen Binding of wogonin to human serum albumin: a common binding site of wogonin in subdomain IIA J. Photochem. Photobiol. B: Biol. 74 2004 39 45 (Pubitemid 38364581)
    • (2004) Journal of Photochemistry and Photobiology B: Biology , vol.74 , Issue.1 , pp. 39-45
    • Tian, J.1    Liu, J.2    Xie, J.3    Yao, X.4    Hu, Z.5    Chen, X.6
  • 119
    • 33746563581 scopus 로고    scopus 로고
    • Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method
    • DOI 10.1016/j.jpba.2006.01.028, PII S0731708506000744
    • Y.-Q. Wang, H.-M. Zhang, and G.-C. Zhang Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method J. Pharm. Biomed. Anal. 41 2006 1041 1046 (Pubitemid 44269078)
    • (2006) Journal of Pharmaceutical and Biomedical Analysis , vol.41 , Issue.3 , pp. 1041-1046
    • Wang, Y.-Q.1    Zhang, H.-M.2    Zhang, G.-C.3
  • 120
    • 44649095723 scopus 로고    scopus 로고
    • Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin
    • DOI 10.1016/j.bmc.2008.05.002, PII S0968089608004215
    • Y.L. Jiang Design, synthesis and spectroscopic studies of resveratrol aliphatic acid ligands of human serum albumin Biorg. Med. Chem. 16 2008 6406 6414 (Pubitemid 351783415)
    • (2008) Bioorganic and Medicinal Chemistry , vol.16 , Issue.12 , pp. 6406-6414
    • Jiang, Y.L.1
  • 121
    • 36749047401 scopus 로고    scopus 로고
    • Interaction of nobiletin with human serum albumin studied using optical spectroscopy and molecular modeling methods
    • DOI 10.1016/j.jlumin.2007.09.029, PII S002223130700292X
    • Y. Yue, Y. Zhang, Y. Li, J. Zhu, J. Qin, and X. Chen Interaction of nobiletin with human serum albumin studied using optical spectroscopy and molecular modelling methods J. Lumin. 128 2008 513 520 (Pubitemid 350212919)
    • (2008) Journal of Luminescence , vol.128 , Issue.3 , pp. 513-520
    • Yue, Y.1    Zhang, Y.2    Li, Y.3    Zhu, J.4    Qin, J.5    Chen, X.6
  • 122
    • 49149090375 scopus 로고    scopus 로고
    • A concise approach to 1,11-didchloro-6-methyl-4′-O-demethyl rebeccamicin (JDC-108) and its binding to human serum albumin: Fluorescence spectroscopy and molecular modelling method
    • F. Cui, L. Qin, G. Zhang, X. Liu, X. Yao, and B. Lei A concise approach to 1,11-didchloro-6-methyl-4′-O-demethyl rebeccamicin (JDC-108) and its binding to human serum albumin: fluorescence spectroscopy and molecular modelling method Bioorg. Med. Chem. 16 2008 7615 7621
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7615-7621
    • Cui, F.1    Qin, L.2    Zhang, G.3    Liu, X.4    Yao, X.5    Lei, B.6
  • 123
    • 62549136995 scopus 로고    scopus 로고
    • Characterization of the interaction between 2′-deoxyuridine and human serum albumin
    • F. Cui, Y. Yan, Q. Zhang, J. Du, X. Yao, G. Qu, and Y. Lu Characterization of the interaction between 2′-deoxyuridine and human serum albumin Carbohydr. Res. 344 2009 642 647
    • (2009) Carbohydr. Res. , vol.344 , pp. 642-647
    • Cui, F.1    Yan, Y.2    Zhang, Q.3    Du, J.4    Yao, X.5    Qu, G.6    Lu, Y.7
  • 126
    • 69249203686 scopus 로고    scopus 로고
    • Molecular modelling an spectroscopic studies on binding of 2,6-bis[4-amino-2-trifluromethyl phenoxy) benzoyl] pyridine to human serum albumin
    • W. He, H. Chen, F. Sheng, and X. Yao Molecular modelling an spectroscopic studies on binding of 2,6-bis[4-amino-2-trifluromethyl phenoxy) benzoyl] pyridine to human serum albumin Spectrochim. Acta A 74 2009 427 433
    • (2009) Spectrochim. Acta A , vol.74 , pp. 427-433
    • He, W.1    Chen, H.2    Sheng, F.3    Yao, X.4
  • 127
    • 27644475219 scopus 로고    scopus 로고
    • Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
    • DOI 10.1016/j.bmc.2005.07.039, PII S0968089605006681
    • Y.-J. Hu, Y. Liu, Z.-B. Pi, and S.-S. Qu Interaction of chromolyn sodium with human serum albumin: a fluorescence quenching study Bioorg. Med. Chem. 13 2005 6609 6614 (Pubitemid 41571205)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.24 , pp. 6609-6614
    • Hu, Y.-J.1    Liu, Y.2    Pi, Z.-B.3    Qu, S.-S.4
  • 128
    • 39149126999 scopus 로고    scopus 로고
    • Probing the binding of morin to human serum albumin by optical spectroscopy
    • Z. Qi, Y. Zhang, F. Liao, Y. Ou-Yang, Y. Liu, and X. Yang Probing the binding of morin to human serum albumin by optical spectroscopy J. Pharm. Biomed. Anal. 46 2008 699 706
    • (2008) J. Pharm. Biomed. Anal. , vol.46 , pp. 699-706
    • Qi, Z.1    Zhang, Y.2    Liao, F.3    Ou-Yang, Y.4    Liu, Y.5    Yang, X.6
  • 129
    • 79951676674 scopus 로고    scopus 로고
    • Exploring the binding mechanism of dihydropyrimidones to human serum albumin: Spectroscopic and molecular modelling techniques
    • G. Wang, D. Wang, X. Li, and Y. Lu Exploring the binding mechanism of dihydropyrimidones to human serum albumin: spectroscopic and molecular modelling techniques Colloids Surf., B 84 2011 272 279
    • (2011) Colloids Surf., B , vol.84 , pp. 272-279
    • Wang, G.1    Wang, D.2    Li, X.3    Lu, Y.4
  • 131
    • 71749110522 scopus 로고    scopus 로고
    • Characterization of the interaction between 8-bromoadenosine with human serum albumin and its analytical application
    • F. Cui, Y. Yan, Q. Zhang, X. Yao, G. Qu, and Y. Lu Characterization of the interaction between 8-bromoadenosine with human serum albumin and its analytical application Spectrochim. Acta Part A: Mol. Biomol. Spectr. 74 2009 964 971
    • (2009) Spectrochim. Acta Part A: Mol. Biomol. Spectr. , vol.74 , pp. 964-971
    • Cui, F.1    Yan, Y.2    Zhang, Q.3    Yao, X.4    Qu, G.5    Lu, Y.6
  • 132
    • 39749154054 scopus 로고    scopus 로고
    • Spectroscopic investigation on the interaction of a cyanine dye with albumins
    • Y. Zhang, Q.-F. Yang, H.-Y. Du, Y. Tang, G.-Z. Xu, and W.-P. Yan Spectroscopic investigation on the interaction of a cyanine dye with albumins Chin. J. Chem. 26 2008 397 401
    • (2008) Chin. J. Chem. , vol.26 , pp. 397-401
    • Zhang, Y.1    Yang, Q.-F.2    Du, H.-Y.3    Tang, Y.4    Xu, G.-Z.5    Yan, W.-P.6
  • 133
    • 16544365706 scopus 로고    scopus 로고
    • Resonance energy transfer between tryptophan-214 in human serum albumin acrylodan, prodan, and promen
    • DOI 10.1023/B:JOPC.0000032655.26249.ba
    • J. González-Jiménez, and M. Cortijo Resonance energy transfer between tryptophan-214 in human serum albumin and Acrylodan Prodan y Promen. Protein J. 23 2004 351 355 (Pubitemid 41399318)
    • (2004) Protein Journal , vol.23 , Issue.5 , pp. 351-355
    • Gonzalez-Jimenez, J.1    Corttjo, M.2
  • 134
    • 59949097010 scopus 로고    scopus 로고
    • Molecular interactions of isoxazolcurcumin with human serum albumin: Spectroscopic and molecular modelling studies
    • B.K. Sahoo, K.S. Gosh, and S. Dasgupta Molecular interactions of isoxazolcurcumin with human serum albumin: spectroscopic and molecular modelling studies Biopolymers 91 2009 108 119
    • (2009) Biopolymers , vol.91 , pp. 108-119
    • Sahoo, B.K.1    Gosh, K.S.2    Dasgupta, S.3
  • 135
    • 77950579365 scopus 로고    scopus 로고
    • Complexes between fluorescent cholic acid derivatives and human serum albumin. Photophysical approach to investigate the binding behaviour
    • J. Rohacova, M.L. Marin, and M.A. Miranda Complexes between fluorescent cholic acid derivatives and human serum albumin. Photophysical approach to investigate the binding behaviour J. Phys. Chem. B 114 2010 4710 4716
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4710-4716
    • Rohacova, J.1    Marin, M.L.2    Miranda, M.A.3
  • 136
    • 76349084691 scopus 로고    scopus 로고
    • Interaction between a novel intramolecular charge transfer fluorescent probe PFEP and human serum albumin
    • D. Ju, S.M. Song, Y.B. Wu, S.M. Shuang, and C. Dong Interaction between a novel intramolecular charge transfer fluorescent probe PFEP and human serum albumin Chin. Chem. Lett. 21 2010 480 483
    • (2010) Chin. Chem. Lett. , vol.21 , pp. 480-483
    • Ju, D.1    Song, S.M.2    Wu, Y.B.3    Shuang, S.M.4    Dong, C.5
  • 137
    • 44749093026 scopus 로고    scopus 로고
    • Binding interaction of indomethacin with human serum albumin
    • M. Bodgan, A. Pirnau, C. Floare, and C. Bugeac Binding interaction of indomethacin with human serum albumin J. Pharm. Biomed. Anal. 47 2008 981 984
    • (2008) J. Pharm. Biomed. Anal. , vol.47 , pp. 981-984
    • Bodgan, M.1    Pirnau, A.2    Floare, C.3    Bugeac, C.4
  • 138
    • 33746211581 scopus 로고    scopus 로고
    • Molecular modelling and spectroscopic studies on the binding of guaiacol to human serum albumin
    • W. He, Y.L. Hongzong Si, Y. Dong, F. Sheng, X. Yao, and Z. Hu Molecular modelling and spectroscopic studies on the binding of guaiacol to human serum albumin J. Photochem. Photobiol. A: Chem. 182 2009 158 167
    • (2009) J. Photochem. Photobiol. A: Chem. , vol.182 , pp. 158-167
    • He, W.1    Hongzong Si, Y.L.2    Dong, Y.3    Sheng, F.4    Yao, X.5    Hu, Z.6
  • 139
    • 38149070870 scopus 로고    scopus 로고
    • In vitro study on the binding of herbicide glyphosate to human serum albumin by optical spectroscopy and molecular modelling
    • Y. Yue, Y. Shang, L. Zhou, J. Qin, and X. Chen In vitro study on the binding of herbicide glyphosate to human serum albumin by optical spectroscopy and molecular modelling J. Photochem. Photobiol. B: Biol. 90 2008 26 32
    • (2008) J. Photochem. Photobiol. B: Biol. , vol.90 , pp. 26-32
    • Yue, Y.1    Shang, Y.2    Zhou, L.3    Qin, J.4    Chen, X.5
  • 140
    • 79955562504 scopus 로고    scopus 로고
    • Interaction of fisetin with human serum albumins by fluorescence, circular dichroism spectroscopy and DFT calculations: Binding parameters and conformational changes
    • I. Matei, S. Ionescu, and M. Hillebrand Interaction of fisetin with human serum albumins by fluorescence, circular dichroism spectroscopy and DFT calculations: binding parameters and conformational changes J. Lumin. 131 2011 1629 1633
    • (2011) J. Lumin. , vol.131 , pp. 1629-1633
    • Matei, I.1    Ionescu, S.2    Hillebrand, M.3
  • 141
    • 79957811971 scopus 로고    scopus 로고
    • Interactions between bovine serum albumin and oxidized sodium alginate in solution
    • C. Gao, M. Liu, J. Chen, and Ch. Chen Interactions between bovine serum albumin and oxidized sodium alginate in solution J. Biomater. Sci. 27 2011 1639 1650
    • (2011) J. Biomater. Sci. , vol.27 , pp. 1639-1650
    • Gao, C.1    Liu, M.2    Chen, J.3    Chen, Ch.4
  • 142
    • 79957626972 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies on the interaction of anticancer drug mitoxantrone with human serum albumin
    • N. Keswani, and N. Kishore Calorimetric and spectroscopic studies on the interaction of anticancer drug mitoxantrone with human serum albumin J. Chem. Thermodyn. 43 2011 1406 1413
    • (2011) J. Chem. Thermodyn. , vol.43 , pp. 1406-1413
    • Keswani, N.1    Kishore, N.2
  • 143
    • 61349190648 scopus 로고    scopus 로고
    • Interaction of alkyl pyridinium chlorides with human serum albumin studied by fluorescence techniques
    • E. Abuin, C. Calderón, and E. Lissi Interaction of alkyl pyridinium chlorides with human serum albumin studied by fluorescence techniques J. Photochem. Photobiol. A: Chem. 195 2008 295 300
    • (2008) J. Photochem. Photobiol. A: Chem. , vol.195 , pp. 295-300
    • Abuin, E.1    Calderón, C.2    Lissi, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.